1116-22-9

Basic information

• Product Name: H-GAMMA-GLU-GLU-OH
• Synonyms: gamma-glutamylglutamate;L-GLUTAMYL-L-GLUTAMIC ACID;L-GAMMA-GLUTAMYL-L-GLUTAMIC ACID;H-GLU(GLU)-OH;H-GLU(GLU-OH)-OH;H-GAMMA-GLU-GLU-OH;GAMMA-GLU-GLU;GAMMA-L-GLUTAMYL-L-GLUTAMIC ACID
• CAS NO: 1116-22-9
• Molecular Formula: C₁₀H₁₆N₂O₇
• Molecular Weight: 276.24
• EINECS: 214-233-2
• Mol File: 1116-22-9.mol

Chemical Properties

• Melting Point: 179-182 °C
• Boiling Point: 419.15°C (rough estimate)
• Flash Point: 355.4oC
• Appearance: White/Powder
• Density: 1.3652 (rough estimate)
• Refractive Index: 1.4550 (estimate)
• Storage Temp.: -15°C
• Solubility: Aqueous Acid (Slightly), Methanol (Slightly), Water (Slightly)
• PKA: 2.21±0.10(Predicted)
• CAS DataBase Reference: H-GAMMA-GLU-GLU-OH(CAS DataBase Reference)
• NIST Chemistry Reference: H-GAMMA-GLU-GLU-OH(1116-22-9)
• EPA Substance Registry System: H-GAMMA-GLU-GLU-OH(1116-22-9)

Safety Data

• Safety Statements: 24/25
• Hazardous Substances Data: 1116-22-9(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
H-GAMMA-GLU-GLU-OH is used as an active pharmaceutical ingredient for its potential therapeutic applications. Its unique structure allows it to interact with various biological targets, making it a promising candidate for the development of new drugs.
Used in Research and Development:
In the field of research and development, H-GAMMA-GLU-GLU-OH serves as a valuable compound for studying the properties and interactions of dipeptides. It can be used to investigate the mechanisms of peptide bond formation, as well as to develop new methods for peptide synthesis and modification.
Used in Cosmetic Industry:
H-GAMMA-GLU-GLU-OH can be utilized as an ingredient in the cosmetic industry, where it may contribute to the development of skincare products with enhanced moisturizing, anti-aging, or protective properties. Its ability to interact with biological molecules could potentially be harnessed to improve the efficacy of cosmetic formulations.
Used in Food Industry:
In the food industry, H-GAMMA-GLU-GLU-OH may find applications as a flavor enhancer, preservative, or additive due to its amino acid composition. Its properties could be exploited to improve the taste, texture, or shelf life of various food products.
Used in Agricultural Industry:
H-GAMMA-GLU-GLU-OH could potentially be employed in the agricultural industry as a component of biostimulants or plant growth promoters. Its interaction with biological molecules may contribute to enhancing plant growth, stress resistance, or nutrient uptake.

Upstream product

• 7365-90-4 benzyloxycarbonyl-α-benzyl-γ-L-glutamyl-L-glutamic acid dibenzyl ester 
• 883451-77-2 N-(O-ethyl-N-benzyloxycarbonyl-L-γ-glutamyl)-L-glutamic acid diethyl ester 
• 4491-17-2 N-(N-benzyloxycarbonyl-L-γ-glutamyl)-L-glutamic acid-1-benzyl ester 
• 72-18-4 L-valine 
• 56-85-9 L-glutamine 
• 56-86-0 L-glutamic acid 
• 4124-76-9 N-(benzyloxycarbonyl)-L-glutamic acid anhydride 
• 16450-41-2 L-glutamic acid diethyl ester 
• 84793-07-7 Fmoc-Glu-OtBu 
• 71989-18-9 Fmoc-Glu(OtBu)-OH 
• 3705-42-8 Cbz-(L)-Glu-OBn 
• 4510-09-2 N-benzyloxycarbonyl-L-glutamic acid-5-hydrazide 
• 13030-09-6 1-benzyl L-glutamate 
• 2768-50-5 dibenzyl L-glutamate 

Downstream Products

• 866557-09-7 (6S)-5,10-dideaza-5,6,7,8-tetrahydropteroyl-L-glutamate-γ-L-glutamate 
• 132487-02-6 (6R)-5,10-dideaza-5,6,7,8-tetrahydropteroyl-L-glutamate-γ-L-glutamate 
• 56-86-0 L-glutamic acid 

Relevant articles and documents

γ-Glutamyl-dipeptides: Easy tools to rapidly probe the stereoelectronic properties of the ionotropic glutamate receptor binding pocket

γ-Glutamyl-dipeptides, built by condensing the distal carboxylate of L-Glu (or D-Glu) onto a series of differently functionalized amino acids, were prepared and used as tools for rapidly probing the stereo-electronic properties of iGluRs, searching for subtype-selective ligands.

Efficient peptide couplings and their use in the synthesis and isolation of a cyclopenta (G) quinazoline trisodium salt

A new method for the synthesis of L-Glutamyl-γ-D-Glutamic acid and its use in the synthesis of (2R)-((4S)-carboxy-4-(4,N-(((6S)-2-(hydroxymethyl)-4-oxo-3,4,7,8-tetrahydro-3H-cyclopenta[g]quinazolin-6-yl)-N-(prop-2-ynyl)amino)benzamido)butanamido)pentanedioic acid, 1 are provided. Also provided is an efficient method for the isolation and purification of the trisodium salt of the abovementioned acid, 2, in a form suitable for long term storage and use in a parenteral dosing form.

Microstructure of poly(γ-glutamic acid) produced by Bacillus subtilis consisting of clusters of D- and L-glutamic acid repeating units

Poly(γ-glutamic acid) (PGA) produced by a strain of Bacillus subtilis was partially hydrolyzed into various oligopeptides so that the dipeptide fraction was isolated by the preparative thin-layer chromatography. HPLC analysis was applied to the detection of each of the four stereoisomers in this fraction using chemically synthesized authentic samples. The fraction consisted of N-γ-D-glutamyl-D-glutamic acid, N-γ-L-glutamyl-L-glutamic acid, N-γ-D-glutamyl-L-glutamic acid, and N-γ-L-glutamyl-D-glutamic acid at a ratio of 5.9:6.0:1.0:1.0. On the basis of this result, a model was proposed for the microstructure of the bacterial PGA, in which D- and L-glutamic acid repeating units are alternately linked in a single chain of the molecule.

Synthesis of (6R)- And (6S)-5,10-dideazatetrahydrofolate oligo-γ-glutamates: Kinetics of multiple glutamate ligations catalyzed by folylpoly-γ-glutamate synthetase

Folylpoly-γ-glutamate synthetase (FPGS, EC 6.3.2.17) catalyzes the ATP-dependent ligation of glutamic acid to reduced folates including (6S)-5,6,7,8-tetrahydrofolate (H4PteGlu), as well as to anticancer drugs such as 5,10-dideaza-5,6,7,8-tetrahydrofolate ((6R)-DDAH 4PteGlu1, (6R)-DDATHF, Lometrexol(tm)). Synthesis of unlabeled mono- and polyglutamates, DDAH4PteGlu n (6R, n = 1-6; 6S, n = 1-2), as well as (6R)-DDAH 4Pte[14C]Glu1, was effected from (6R)- or (6S)-5,10-dideazatetrahydropteroyl azide and glutamic acid, H-Glu-γ- Glun-y-Glu-OH (n = 0-4), or [14C]glutamic acid, respectively. These compounds were evaluated as FPGS substrates to determine steady-state kinetic constants. Michaelis-Menten kinetics were observed for (6-R)-DDAH4PteGlu1, the isomer corresponding to H 4PteGlu, whereas marked substrate inhibition was observed for (6S)-DDAH4PteGlun (n = 1-2) and (6R)-DDAH 4PteGlun (n = 2-5), but not (6.R)-DDAH 4PteGlu6. Multiple ligation of glutamate renders a quantitative analysis of these data difficult. However, approximate values of KM = 0.65-1.6 μM and K1, = 144-417 μM for DDAH 4PteGln were obtained using a simple kinetic model. The Royal Society of Chemistry 2005.

Effective formation of di- and tri-gamma-glutamates by gamma-glutamyltranspeptidase.

Using gamma-glutamyltranspeptidase, conditions for di- and tri-gamma-glutamates synthesis were studied with glutamine and glutamic acid esters as substrates. The reactivity of amino acid esters was higher than for free ones. The efficient conditions were the combination of glutamine ethyl and glutamate diethyl esters with a molar ratio of 1/10 at pH 7-8.

Action of Glutaminase in a Model System of a Soy Sauce Fermentation

A model system was employed to investigate the role of glutaminase in soy sauce fermentation.In this system, a soybean protein was used as the starting material and a water extract of wheat bran koji was used as the enzyme preparation containing proteinases, peptidases, glutaminases and so on.A soybean protein was digested with the enzyme preparation. γ-Glutamylserine, γ-glutamylglutamic acid and γ-glutamylalanine were isolated from an acidic fraction of the soybean protein digest.The addition of the purified glutaminase from Aspergillus oryzae led to more production of glutamic acid and γ-glutamyl peptide and less production of glutamine and pyroglutamic acid. γ-Glutamyltranspeptidase activity and γ-glutamyl peptide(s) were also detected in a partical soy sauce mash.

Aspartyl and Glutamyl Peptides and the Acidic Cysteine Derivatives in Asparagus (Asparagus officinalis) Shoots

γ-Glutamyl peptides and acidic cysteine derivatives were found in low concentrations in asparagus shoots.However, the presence of α- and β-aspartylaspartic acid, α-aspartylglutamic acid, γ-glutamylaspartic acid, γ-glutamylglutamic acid, γ-glutamyltyrosine, S-(2-carboxy-n-propyl)-L-cysteine and S-(1,2-dicarboxyethyl)-L-cysteine was demonstrated in the acidic amino acids fraction of asparagus shoots.

Synthesis of γ-Glutamyl Peptides Catalyzed by Transamidase from Bacillus natto

Crude ammonium sulfate fraction of a cell free extract from Bacillus natto contained an enzyme (or enzymes) which catalyzed the transamidation reaction specific for glutamine.Both L- and D-isomers of glutamine were active as substrate.On incubation of L- or D-glutamine with the enzyme preparation, two peptides consisting of glutamic acid and glutamine were formed.The main component of the peptides was readily isolated by ion-exchange chromatography and identified as γ-glutamylglutamine by paper chromatography and by paper electrophoresis using authentic peptides.The optical configuration of the amino acid residues in the dipeptide was determined by digestion of the acid hydrolyzate with L-glutamic acid decarboxylase, and the result showed that the dipeptide obtained from L-glutamine was a L-L isomer, while the dipeptide from D-glutamine was a D-D isomer.